A0A1N6YTH4 · A0A1N6YTH4_9GAMM

  • Protein
    Fatty acid oxidation complex subunit alpha
  • Gene
    fadB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

Function

function

Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.

Catalytic activity

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Features

Showing features for site, binding site, active site.

TypeIDPosition(s)Description
Site119Important for catalytic activity
Site139Important for catalytic activity
Binding site296substrate
Binding site325NAD+ (UniProtKB | ChEBI)
Binding site344NAD+ (UniProtKB | ChEBI)
Binding site401-403NAD+ (UniProtKB | ChEBI)
Binding site408NAD+ (UniProtKB | ChEBI)
Binding site430NAD+ (UniProtKB | ChEBI)
Active site451For 3-hydroxyacyl-CoA dehydrogenase activity
Binding site454NAD+ (UniProtKB | ChEBI)
Binding site501substrate
Binding site661substrate

GO annotations

AspectTerm
Cellular Componentfatty acid beta-oxidation multienzyme complex
Molecular Function3-hydroxyacyl-CoA dehydrogenase activity
Molecular Function3-hydroxybutyryl-CoA epimerase activity
Molecular Functiondelta(3)-delta(2)-enoyl-CoA isomerase activity
Molecular Functionenoyl-CoA hydratase activity
Molecular FunctionNAD+ binding
Biological Processfatty acid beta-oxidation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Fatty acid oxidation complex subunit alpha

Including 2 domains:

  • Recommended name
    Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase
  • EC number
  • Recommended name
    3-hydroxyacyl-CoA dehydrogenase
  • EC number

Gene names

    • Name
      fadB
    • ORF names
      SAMN05880558_109176

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • RU39B
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Aeromonadales > Aeromonadaceae > Aeromonas

Accessions

  • Primary accession
    A0A1N6YTH4

Proteomes

Interaction

Subunit

Heterotetramer of two alpha chains (FadB) and two beta chains (FadA).

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-189Enoyl-CoA hydratase/isomerase
Region311-7153-hydroxyacyl-CoA dehydrogenase
Domain317-4953-hydroxyacyl-CoA dehydrogenase NAD binding
Domain497-5933-hydroxyacyl-CoA dehydrogenase C-terminal
Domain630-7103-hydroxyacyl-CoA dehydrogenase C-terminal

Sequence similarities

In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    715
  • Mass (Da)
    76,360
  • Last updated
    2017-03-15 v1
  • Checksum
    86757B1542764693
MIYQGDTLTVRYLESGIAELRFDAPGSVNKLDRATLLSLGDAIAALQQERELKGLILTSGKDAFIVGADITEFLALFALPDADLLGWLKKANDIFCALEDLPVPTLSAIRGHALGGGCETILSTDLRLADTTAKIGLPETKLGIMPGFGGTVRLPRVIGADNALEWITSGKDYRAEEALKVGAVDAVVAPDALQNAALQMIKDAISGKLDWQGRRAAKTSPLRLSKMEAMMSFTTAAGMVAAVAGKHYPAPMAAVKTVEAAAGMGRDDALAAEAATFIKLAKTDVAKALVGIFLGDQYIKGLAKQSAKKASKATEHAAVLGAGIMGGGIAYQSASKGIPAIMKDINEKALQLGMSEATKLLNGQLEKGRIDGIKMGQVLSSITPTLSYDSVKGVDLVVEAVVENPKVKEAVLSEVEGLLGDDTVLASNTSTIPISLLANSLKRPENFCGMHFFNPVHRMPLVEIIRGEKTSEETIDRVVAYAAAMGKSPVVVNDCPGFFVNRVLFPYFFGFNKLVADGADFAAVDKVMEKEFGWPMGPAYLLDVVGIDTGHHAGDVMAQGFPARMNKEGRTAIDVMFEAGRFGQKNGKGFYAYESDSKGKPKKVADPASYQLLEPIAKPRQEFDKETLIARMMIPMINEVVLCLEEGIIATPAEADLALVYGLGFPPFRGGVFRYLDALGLDAYVAMADRFANLGPLYRVSDKLREMAAQGKTFY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FTMJ01000009
EMBL· GenBank· DDBJ
SIR17842.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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